Next Article in Journal
Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes
Next Article in Special Issue
Effects of Honokiol on CYP450 Activity and Transporter mRNA Expression in Type 2 Diabetic Rats
Previous Article in Journal
Applications of Alternative Nucleases in the Age of CRISPR/Cas9
Previous Article in Special Issue
Inhibitory Effects of Trapping Agents of Sulfur Drug Reactive Intermediates against Major Human Cytochrome P450 Isoforms
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2017, 18(12), 2564;

Buprofezin Is Metabolized by CYP353D1v2, a Cytochrome P450 Associated with Imidacloprid Resistance in Laodelphax striatellus

The Key Laboratory of Monitoring and Management of Plant Diseases and Insects, Department of Entomology, College of Plant Protection, Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, China
College of Crop Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China
Authors to whom correspondence should be addressed.
Received: 22 September 2017 / Revised: 14 November 2017 / Accepted: 20 November 2017 / Published: 29 November 2017
(This article belongs to the Special Issue Cytochromes P450: Drug Metabolism and Bioactivation)
Full-Text   |   PDF [2059 KB, uploaded 29 November 2017]   |  


CYP353D1v2 is a cytochrome P450 related to imidacloprid resistance in Laodelphax striatellus. This work was conducted to examine the ability of CYP353D1v2 to metabolize other insecticides. Carbon monoxide difference spectra analysis indicates that CYP353D1v2 was successfully expressed in insect cell Sf9. The catalytic activity of CYP353D1v2 relating to degrading buprofezin, chlorpyrifos, and deltamethrin was tested by measuring substrate depletion and analyzing the formation of metabolites. The results showed the nicotinamide–adenine dinucleotide phosphate (NADPH)-dependent depletion of buprofezin (eluting at 8.7 min) and parallel formation of an unknown metabolite (eluting 9.5 min). However, CYP353D1v2 is unable to metabolize deltamethrin and chlorpyrifos. The recombinant CYP353D1v2 protein efficiently catalyzed the model substrate p-nitroanisole with a maximum velocity of 9.24 nmol/min/mg of protein and a Michaelis constant of Km = 6.21 µM. In addition, imidacloprid was metabolized in vitro by the recombinant CYP353D1v2 microsomes (catalytic constant Kcat) 0.064 pmol/min/pmol P450, Km = 6.41 µM. The mass spectrum of UPLC-MS analysis shows that the metabolite was a product of buprofezin, which was buprofezin sulfone. This result provided direct evidence that L. striatellus cytochrome P450 CYP353D1v2 is capable of metabolizing imidacloprid and buprofezin. View Full-Text
Keywords: buprofezin; Cytochrome P450; functional expression; insecticide metabolism; cross-resistance buprofezin; Cytochrome P450; functional expression; insecticide metabolism; cross-resistance

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Elzaki, M.E.A.; Miah, M.A.; Han, Z. Buprofezin Is Metabolized by CYP353D1v2, a Cytochrome P450 Associated with Imidacloprid Resistance in Laodelphax striatellus. Int. J. Mol. Sci. 2017, 18, 2564.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top